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Literature summary extracted from

  • Chan, S.I.; Li, P.M.
    Cytochrome c oxidase: understanding natures design of a proton pump (1990), Biochemistry, 29, 1-12.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
7.1.1.9
-
 Paracoccus denitrificans

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
7.1.1.9 Cu CuB located in subunit I, electron flow from ferrocytochrome c to binuclear center Bacteria
7.1.1.9 Cu CuA located in subunit II, binding of O2 and reduction Bacteria
7.1.1.9 Cu CuB located in subunit I, electron flow from ferrocytochrome c to binuclear center eukaryota
7.1.1.9 Cu CuA located in subunit II, binding of O2 and reduction eukaryota
7.1.1.9 Cu
-
 Mammalia
7.1.1.9 Cu CuB located in subunit I, electron flow from ferrocytochrome c to binuclear center Paracoccus denitrificans
7.1.1.9 Cu CuA located in subunit II, binding of O2 and reduction Paracoccus denitrificans
7.1.1.9 Fe
-
 Bacteria
7.1.1.9 Fe
-
 eukaryota
7.1.1.9 Fe
-
 Mammalia
7.1.1.9 Mg
-
 Mammalia
7.1.1.9 additional information all redox-active metal centers are contained in subunits I and II eukaryota

Organism

EC Number Organism UniProt Comment Textmining
7.1.1.9 Bacteria
-
-
-
7.1.1.9 eukaryota
-
-
-
7.1.1.9 Mammalia
-
-
-
7.1.1.9 Paracoccus denitrificans
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
7.1.1.9 4 ferrocytochrome c + O2 + 8 H+[side 1] = 4 ferricytochrome c + 2 H2O + 4+[side 2] mechanism of O2 reduction eukaryota
a
7.1.1.9 4 ferrocytochrome c + O2 + 8 H+[side 1] = 4 ferricytochrome c + 2 H2O + 4+[side 2] mechanism of O2 reduction Bacteria
a
7.1.1.9 4 ferrocytochrome c + O2 + 8 H+[side 1] = 4 ferricytochrome c + 2 H2O + 4+[side 2] proposal for complete turnover cycle, i.e. intramolecular electron transfer, O2 reduction and proton pumping eukaryota
a
7.1.1.9 4 ferrocytochrome c + O2 + 8 H+[side 1] = 4 ferricytochrome c + 2 H2O + 4+[side 2] proposal for complete turnover cycle, i.e. intramolecular electron transfer, O2 reduction and proton pumping Bacteria
a
7.1.1.9 4 ferrocytochrome c + O2 + 8 H+[side 1] = 4 ferricytochrome c + 2 H2O + 4+[side 2] mechanism of proton pumping eukaryota
a
7.1.1.9 4 ferrocytochrome c + O2 + 8 H+[side 1] = 4 ferricytochrome c + 2 H2O + 4+[side 2] mechanism of proton pumping Bacteria
a
7.1.1.9 4 ferrocytochrome c + O2 + 8 H+[side 1] = 4 ferricytochrome c + 2 H2O + 4+[side 2] mechanism of proton pumping Mammalia
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
7.1.1.9 ferrocytochrome c + O2
-
 Paracoccus denitrificans ferricytochrome c + H2O
-
 ?
7.1.1.9 ferrocytochrome c + O2 proton translocation across eukaryotic mitochondrial and prokyryotic cytoplasmic membrane, overview proposed mechanims eukaryota ferricytochrome c + H2O
-
 ?
7.1.1.9 ferrocytochrome c + O2 proton translocation across eukaryotic mitochondrial and prokyryotic cytoplasmic membrane, overview proposed mechanims Bacteria ferricytochrome c + H2O
-
 ?
7.1.1.9 ferrocytochrome c + O2 + H+
-
 Bacteria ferricytochrome c + H2O
-
 r
7.1.1.9 ferrocytochrome c + O2 + H+
-
 eukaryota ferricytochrome c + H2O
-
 r

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
7.1.1.9 30 600 ferrocytochrome c
-
 eukaryota
7.1.1.9 30 600 ferrocytochrome c
-
 Bacteria

pH Range

EC Number pH Minimum pH Maximum Comment Organism
7.1.1.9 additional information
-
 redox potential of cytochrome a is pH dependent eukaryota

Cofactor

EC Number Cofactor Comment Organism Structure
7.1.1.9 heme a
-
 Paracoccus denitrificans
7.1.1.9 heme a
-
 Mammalia
7.1.1.9 heme a located in subunit I eukaryota
7.1.1.9 heme a located in subunit I Bacteria
7.1.1.9 Heme a3
-
 Mammalia
7.1.1.9 Heme a3 located in subunit I eukaryota
7.1.1.9 Heme a3 located in subunit I Bacteria
7.1.1.9 Heme a3 located in subunit I Paracoccus denitrificans